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  • Time Factors  (151)
  • *Ecosystem
  • Protein Structure, Tertiary
  • Rats
  • Nature Publishing Group (NPG)  (271)
  • American Association for the Advancement of Science (AAAS)  (97)
  • 2015-2019  (368)
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  • Nature Publishing Group (NPG)  (271)
  • American Association for the Advancement of Science (AAAS)  (97)
  • MDPI AG  (1)
Years
Year
  • 1
    Publication Date: 2015-04-23
    Description: The current outbreak of Ebola virus in West Africa is unprecedented, causing more cases and fatalities than all previous outbreaks combined, and has yet to be controlled. Several post-exposure interventions have been employed under compassionate use to treat patients repatriated to Europe and the United States. However, the in vivo efficacy of these interventions against the new outbreak strain of Ebola virus is unknown. Here we show that lipid-nanoparticle-encapsulated short interfering RNAs (siRNAs) rapidly adapted to target the Makona outbreak strain of Ebola virus are able to protect 100% of rhesus monkeys against lethal challenge when treatment was initiated at 3 days after exposure while animals were viraemic and clinically ill. Although all infected animals showed evidence of advanced disease including abnormal haematology, blood chemistry and coagulopathy, siRNA-treated animals had milder clinical features and fully recovered, while the untreated control animals succumbed to the disease. These results represent the first, to our knowledge, successful demonstration of therapeutic anti-Ebola virus efficacy against the new outbreak strain in nonhuman primates and highlight the rapid development of lipid-nanoparticle-delivered siRNA as a countermeasure against this highly lethal human disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4467030/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4467030/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thi, Emily P -- Mire, Chad E -- Lee, Amy C H -- Geisbert, Joan B -- Zhou, Joy Z -- Agans, Krystle N -- Snead, Nicholas M -- Deer, Daniel J -- Barnard, Trisha R -- Fenton, Karla A -- MacLachlan, Ian -- Geisbert, Thomas W -- U19 AI109711/AI/NIAID NIH HHS/ -- U19AI109711/AI/NIAID NIH HHS/ -- England -- Nature. 2015 May 21;521(7552):362-5. doi: 10.1038/nature14442. Epub 2015 Apr 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tekmira Pharmaceuticals, Burnaby, British Columbia V5J 5J8, Canada. ; 1] Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas 77550, USA [2] Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas 77550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25901685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Disease Models, Animal ; Ebolavirus/classification/*drug effects/*genetics ; Female ; Hemorrhagic Fever, Ebola/pathology/prevention & control/*therapy/*virology ; Humans ; Macaca mulatta/virology ; Male ; Nanoparticles/*administration & dosage ; RNA, Small Interfering/*administration & dosage/pharmacology/*therapeutic use ; Survival Analysis ; Time Factors ; Treatment Outcome ; Viral Load/drug effects
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  • 2
    Publication Date: 2015-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Limardo, Alexander J -- Worden, Alexandra Z -- England -- Nature. 2015 Jun 4;522(7554):36-7. doi: 10.1038/nature14530. Epub 2015 May 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ocean Sciences, University of California, Santa Cruz, California 95064, USA, and at the Monterey Bay Aquarium Research Institute, Moss Landing, California. ; 1] Department of Ocean Sciences, University of California, Santa Cruz, California 95064, USA, and at the Monterey Bay Aquarium Research Institute, Moss Landing, California. [2] Canadian Institute for Advanced Research, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26017309" target="_blank"〉PubMed〈/a〉
    Keywords: Diatoms/*metabolism/*microbiology ; *Ecosystem ; Indoleacetic Acids/*metabolism ; Phytoplankton/*metabolism/*microbiology ; Rhodobacteraceae/*metabolism
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  • 3
    Publication Date: 2015-09-22
    Description: Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 A. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Jingpeng -- Li, Wanqiu -- Zhao, Qiancheng -- Li, Ningning -- Chen, Maofei -- Zhi, Peng -- Li, Ruochong -- Gao, Ning -- Xiao, Bailong -- Yang, Maojun -- England -- Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China. ; Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. ; Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China. ; IDG/McGovern Institute for Brain Research, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26390154" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; *Cryoelectron Microscopy ; Electric Conductivity ; Ion Channel Gating ; Ion Channels/*chemistry/metabolism/*ultrastructure ; Mice ; Models, Molecular ; Pliability ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism
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  • 4
    Publication Date: 2015-07-24
    Description: Bacteria secrete peptides and proteins to communicate, to poison competitors, and to manipulate host cells. Among the various protein-translocation machineries, the peptidase-containing ATP-binding cassette transporters (PCATs) are appealingly simple. Each PCAT contains two peptidase domains that cleave the secretion signal from the substrate, two transmembrane domains that form a translocation pathway, and two nucleotide-binding domains that hydrolyse ATP. In Gram-positive bacteria, PCATs function both as maturation proteases and exporters for quorum-sensing or antimicrobial polypeptides. In Gram-negative bacteria, PCATs interact with two other membrane proteins to form the type 1 secretion system. Here we present crystal structures of PCAT1 from Clostridium thermocellum in two different conformations. These structures, accompanied by biochemical data, show that the translocation pathway is a large alpha-helical barrel sufficient to accommodate small folded proteins. ATP binding alternates access to the transmembrane pathway and also regulates the protease activity, thereby coupling substrate processing to translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, David Yin-wei -- Huang, Shuo -- Chen, Jue -- Howard Hughes Medical Institute/ -- England -- Nature. 2015 Jul 23;523(7561):425-30. doi: 10.1038/nature14623.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Laboratory of Membrane Biology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA [2] Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA. ; Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26201595" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/deficiency/metabolism ; Clostridium thermocellum/*chemistry ; Crystallography, X-Ray ; Models, Molecular ; Peptides/*metabolism/secretion ; Protein Binding ; Protein Multimerization ; Protein Structure, Tertiary ; Structure-Activity Relationship
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  • 5
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    Nature Publishing Group (NPG)
    Publication Date: 2015-11-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geddes, Linda -- England -- Nature. 2015 Nov 5;527(7576):22-5. doi: 10.1038/527022a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26536940" target="_blank"〉PubMed〈/a〉
    Keywords: Attention Deficit Disorder with ; Hyperactivity/diagnosis/physiopathology/psychology ; Autism Spectrum Disorder/diagnosis/physiopathology/psychology ; Brain/blood supply/*growth & development/*physiology ; *Child Development ; Child, Preschool ; Electroencephalography ; Electromyography ; Eye Movements/physiology ; Female ; Humans ; Infant ; Infant Behavior/*physiology/*psychology ; *Laboratories ; London ; Magnetic Resonance Imaging ; Male ; Mirror Neurons ; Neuroimaging ; Personality ; Spectroscopy, Near-Infrared ; Time Factors
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  • 6
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    Nature Publishing Group (NPG)
    Publication Date: 2015-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉England -- Nature. 2015 May 28;521(7553):394. doi: 10.1038/521394a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26017406" target="_blank"〉PubMed〈/a〉
    Keywords: *Bibliometrics/history ; History, 19th Century ; History, 20th Century ; History, 21st Century ; Research/*history ; Time Factors
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  • 7
    Publication Date: 2015-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Oliveira, Joao Ricardo Mendes -- England -- Nature. 2015 Oct 22;526(7574):506. doi: 10.1038/526506e.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Federal University of Pernambuco, Recife, Brazil.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26490608" target="_blank"〉PubMed〈/a〉
    Keywords: Brazil ; Financing, Organized/*economics/*organization & administration ; Research Personnel/*economics ; Research Support as Topic/*economics/*organization & administration ; Time Factors
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  • 8
    Publication Date: 2015-07-15
    Description: Surface polysaccharides are important for bacterial interactions with multicellular organisms, and some are virulence factors in pathogens. In the legume-rhizobium symbiosis, bacterial exopolysaccharides (EPS) are essential for the development of infected root nodules. We have identified a gene in Lotus japonicus, Epr3, encoding a receptor-like kinase that controls this infection. We show that epr3 mutants are defective in perception of purified EPS, and that EPR3 binds EPS directly and distinguishes compatible and incompatible EPS in bacterial competition studies. Expression of Epr3 in epidermal cells within the susceptible root zone shows that the protein is involved in bacterial entry, while rhizobial and plant mutant studies suggest that Epr3 regulates bacterial passage through the plant's epidermal cell layer. Finally, we show that Epr3 expression is inducible and dependent on host perception of bacterial nodulation (Nod) factors. Plant-bacterial compatibility and bacterial access to legume roots is thus regulated by a two-stage mechanism involving sequential receptor-mediated recognition of Nod factor and EPS signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaharada, Y -- Kelly, S -- Nielsen, M Wibroe -- Hjuler, C T -- Gysel, K -- Muszynski, A -- Carlson, R W -- Thygesen, M B -- Sandal, N -- Asmussen, M H -- Vinther, M -- Andersen, S U -- Krusell, L -- Thirup, S -- Jensen, K J -- Ronson, C W -- Blaise, M -- Radutoiu, S -- Stougaard, J -- England -- Nature. 2015 Jul 16;523(7560):308-12. doi: 10.1038/nature14611. Epub 2015 Jul 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000 C, Denmark. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000 C, Denmark [3] Department of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Chemistry, University of Copenhagen, Frederiksberg 1871 C, Denmark. ; Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26153863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Sequence ; Lipopolysaccharides/chemistry/*metabolism ; Lotus/genetics/*metabolism/*microbiology ; Molecular Sequence Data ; Mutation/genetics ; Phenotype ; Plant Epidermis/metabolism/microbiology ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Root Nodulation ; Protein Kinases/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Rhizobium/*metabolism ; Root Nodules, Plant/metabolism/microbiology ; Signal Transduction ; Species Specificity ; Suppression, Genetic/genetics ; *Symbiosis
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  • 9
    Publication Date: 2015-05-29
    Description: Robots have transformed many industries, most notably manufacturing, and have the power to deliver tremendous benefits to society, such as in search and rescue, disaster response, health care and transportation. They are also invaluable tools for scientific exploration in environments inaccessible to humans, from distant planets to deep oceans. A major obstacle to their widespread adoption in more complex environments outside factories is their fragility. Whereas animals can quickly adapt to injuries, current robots cannot 'think outside the box' to find a compensatory behaviour when they are damaged: they are limited to their pre-specified self-sensing abilities, can diagnose only anticipated failure modes, and require a pre-programmed contingency plan for every type of potential damage, an impracticality for complex robots. A promising approach to reducing robot fragility involves having robots learn appropriate behaviours in response to damage, but current techniques are slow even with small, constrained search spaces. Here we introduce an intelligent trial-and-error algorithm that allows robots to adapt to damage in less than two minutes in large search spaces without requiring self-diagnosis or pre-specified contingency plans. Before the robot is deployed, it uses a novel technique to create a detailed map of the space of high-performing behaviours. This map represents the robot's prior knowledge about what behaviours it can perform and their value. When the robot is damaged, it uses this prior knowledge to guide a trial-and-error learning algorithm that conducts intelligent experiments to rapidly discover a behaviour that compensates for the damage. Experiments reveal successful adaptations for a legged robot injured in five different ways, including damaged, broken, and missing legs, and for a robotic arm with joints broken in 14 different ways. This new algorithm will enable more robust, effective, autonomous robots, and may shed light on the principles that animals use to adapt to injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cully, Antoine -- Clune, Jeff -- Tarapore, Danesh -- Mouret, Jean-Baptiste -- England -- Nature. 2015 May 28;521(7553):503-7. doi: 10.1038/nature14422.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Sorbonne Universites, Universite Pierre et Marie Curie (UPMC), Paris 06, UMR 7222, Institut des Systemes Intelligents et de Robotique (ISIR), F-75005, Paris, France [2] CNRS, UMR 7222, Institut des Systemes Intelligents et de Robotique (ISIR), F-75005, Paris, France. ; Department of Computer Science, University of Wyoming, Laramie, Wyoming 82071, USA. ; 1] Sorbonne Universites, Universite Pierre et Marie Curie (UPMC), Paris 06, UMR 7222, Institut des Systemes Intelligents et de Robotique (ISIR), F-75005, Paris, France [2] CNRS, UMR 7222, Institut des Systemes Intelligents et de Robotique (ISIR), F-75005, Paris, France [3] Inria, Team Larsen, Villers-les-Nancy, F-54600, France [4] CNRS, Loria, UMR 7503, Vandoeuvre-les-Nancy, F-54500, France [5] Universite de Lorraine, Loria, UMR 7503, Vandoeuvre-les-Nancy, F-54500, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26017452" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Algorithms ; Animals ; *Artificial Intelligence ; Behavior, Animal ; Biomimetics/*methods ; Dogs ; Extremities/*injuries/physiopathology ; Motor Skills ; Robotics/*instrumentation/*methods ; Time Factors
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  • 10
    Publication Date: 2015-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zanne, Amy E -- Tank, David C -- Cornwell, William K -- Eastman, Jonathan M -- Smith, Stephen A -- FitzJohn, Richard G -- McGlinn, Daniel J -- O'Meara, Brian C -- Moles, Angela T -- Reich, Peter B -- Royer, Dana L -- Soltis, Douglas E -- Stevens, Peter F -- Westoby, Mark -- Wright, Ian J -- Aarssen, Lonnie -- Bertin, Robert I -- Calaminus, Andre -- Govaerts, Rafael -- Hemmings, Frank -- Leishman, Michelle R -- Oleksyn, Jacek -- Soltis, Pamela S -- Swenson, Nathan G -- Warman, Laura -- Beaulieu, Jeremy M -- England -- Nature. 2015 May 21;521(7552):E6-7. doi: 10.1038/nature14394.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Biological Sciences, George Washington University, Washington DC 20052, USA. [2] Center for Conservation and Sustainable Development, Missouri Botanical Garden, St Louis, Missouri 63121, USA. ; 1] Department of Biological Sciences, University of Idaho, Moscow, Idaho 83844, USA. [2] Institute for Bioinformatics and Evolutionary Studies, University of Idaho, Moscow, Idaho 83844, USA. ; 1] Department of Ecological Sciences, Systems Ecology, de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands. [2] Evolution &Ecology Research Centre, School of Biological, Earth and Environmental Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia. ; Department of Ecology and Evolutionary Biology, University of Michigan, Ann Arbor, Michigan 48109, USA. ; 1] Department of Zoology and Biodiversity Research Centre, University of British Columbia, Vancouver, British Columbia V6T1Z4, Canada. [2] Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia. ; Department of Biology, College of Charleston, Charleston, South Carolina 29424, USA. ; Department of Ecology and Evolutionary Biology, University of Tennessee, Knoxville, Tennessee 37996, USA. ; Evolution &Ecology Research Centre, School of Biological, Earth and Environmental Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia. ; 1] Department of Forest Resources, University of Minnesota, St Paul, Minnesota 55108, USA. [2] Hawkesbury Institute for the Environment, University of Western Sydney, Penrith, New South Wales 2751, Australia. ; Department of Earth and Environmental Sciences, Wesleyan University, Middletown, Connecticut 06459, USA. ; 1] Department of Biology, University of Florida, Gainesville, Florida 32611, USA. [2] Florida Museum of Natural History, University of Florida, Gainesville, Florida 32611, USA. [3] Genetics Institute, University of Florida, Gainesville, Florida 32611, USA. ; Department of Biology, University of Missouri-St Louis, St Louis, Missouri 63121, USA. ; Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia. ; Department of Biology, Queen's University, Kingston, Ontario K7L 3N6, Canada. ; Department of Biology, College of the Holy Cross, Worcester, Massachusetts 01610, USA. ; Department of Biology, University of Florida, Gainesville, Florida 32611, USA. ; Royal Botanic Gardens, Kew, Richmond TW9 3AB, UK. ; 1] Department of Forest Resources, University of Minnesota, St Paul, Minnesota 55108, USA. [2] Polish Academy of Sciences, Institute of Dendrology, 62-035 Kornik, Poland. ; 1] Florida Museum of Natural History, University of Florida, Gainesville, Florida 32611, USA. [2] Genetics Institute, University of Florida, Gainesville, Florida 32611, USA. ; Department of Plant Biology and Ecology, Evolutionary Biology and Behavior, Program, Michigan State University, East Lansing, Michigan 48824, USA. ; 1] Evolution &Ecology Research Centre, School of Biological, Earth and Environmental Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia. [2] Institute of Pacific Islands Forestry, USDA Forest Service, Hilo, Hawaii 96720, USA. ; National Institute for Mathematical &Biological Synthesis, University of Tennessee, Knoxville, Tennessee 37996, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25993971" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*anatomy & histology/*physiology ; *Biological Evolution ; *Cold Climate ; *Ecosystem ; *Freezing ; Xylem/*anatomy & histology
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